- Alcoholysis of epsilon-decalactone with polyethylene glycol-modified lipase in 1,1,1-trichloroethane.
Alcoholysis of epsilon-decalactone with polyethylene glycol-modified lipase in 1,1,1-trichloroethane.
Biochemical and biophysical research communications (1994-02-28)
M Furukawa, Y Kodera, T Uemura, M Hiroto, A Matsushima, H Kuno, H Matsushita, Y Inada
PMID8123042
ABSTRACT
Lipase from Pseudomonas cepacia was modified with 2,4-bis[O-methoxypoly(ethylene glycol)]-6-chloro-s-triazine, activated PEG2, to form PEG-lipase. The PEG-lipase is soluble and active in organic solvents. It catalyzes alcoholysis of racemic epsilon-decalactone with ethanol in 1,1,1-trichloroethane to form (R)-hydroxydecanoic acid ethyl ester. No alcoholysis of (S)-decalactone takes place. These results were discussed in relation to carbon number of n-alcohol, optimum temperature and comparison with modified and non-modified lipases.